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CATH Superfamily 3.10.110.10

Ubiquitin Conjugating Enzyme

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Ubiquitin Conjugating Enzyme
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 6093: E3 ubiquitin-protein ligase RNF25

There are 3 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Non-specific serine/threonine protein kinase. [EC: 2.7.11.1]
ATP + a protein = ADP + a phosphoprotein.
  • This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date.
  • Formerly EC 2.7.1.37 and EC 2.7.1.70.
 10 B5VGG1 B5VGG1 N1P8J5 N1P8J5 P15442 P15442 Q75JN1 Q75JN1 Q9HGN1 Q9HGN1
RING-type E3 ubiquitin transferase. [EC: 2.3.2.27]
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
  • The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin an the epsilon-amino group of an L-lysine residue of the acceptor protein.
  • The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26).
  • RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies.
  • Formerly EC 6.3.2.19 and EC 6.3.2.21.
 6 Q5E9N3 Q5E9N3 Q96BH1 Q96BH1 Q9QZR0 Q9QZR0
[Elongation factor 2] kinase. [EC: 2.7.11.20]
ATP + [elongation factor 2] = ADP + [elongation factor 2] phosphate.
  • Requires calmodulin for activity.
  • Can also be phosphorylated by the catalytic subunit of EC 2.7.11.11.
  • Elongation factor 2 is phosphorylated in several cell types in response to various growth factors, hormones and other stimuli that raise intracellular Ca(2+).
 4 A0A0B4KHX7 A0A0B4KHX7 Q9V9X8 Q9V9X8
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